Literature DB >> 8764009

Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly.

P S Pendergrast1, D Morrison, W P Tansey, N Hernandez.   

Abstract

The human immunodeficiency virus type 1 promoter generates two types of RNA molecules, full-length transcripts and short transcripts. Synthesis of the short transcripts depends on the inducer of short transcripts (IST), an element located downstream of the start site. In the presence of the viral activator Tat, the synthesis of full-length transcripts is up-regulated while that of short transcripts is down-regulated. Full-length and short transcripts are probably generated by different types of transcription complexes. The first is IST independent, capable of efficient elongation, and up-regulated by Tat. The second is IST dependent, incapable of efficient elongation, and down-regulated by Tat. We have used an in vivo assay to assess the role of TBP in human immunodeficiency virus type I transcription and to test the effect of mutations in TBP on synthesis of full-length and short transcripts. We find that TBP bound to the TATA box is required for the synthesis of short and full-length transcripts as well as for Tat activation and that both yeast TBP and the carboxy-terminal domain of human TBP can replace full-length human TBP for these processes. Mutations in TBP affect the synthesis of short and full-length transcripts as well as Tat activation similarly, and these effects correlate with the previously described effects of these mutations on binding of TBP to the TBP-associated factor TAFII250 in vitro. Together, these results suggest that if short and full-length transcripts are generated by variant transcription complexes, these complexes use TBP similarly, probably as part of the TFIID complex.

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Year:  1996        PMID: 8764009      PMCID: PMC190456     

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  55 in total

1.  HIV-1 Tat overcomes inefficient transcriptional elongation in vitro.

Authors:  M F Laspia; P Wendel; M B Mathews
Journal:  J Mol Biol       Date:  1993-08-05       Impact factor: 5.469

2.  Co-crystal structure of TBP recognizing the minor groove of a TATA element.

Authors:  J L Kim; D B Nikolov; S K Burley
Journal:  Nature       Date:  1993-10-07       Impact factor: 49.962

3.  Crystal structure of a yeast TBP/TATA-box complex.

Authors:  Y Kim; J H Geiger; S Hahn; P B Sigler
Journal:  Nature       Date:  1993-10-07       Impact factor: 49.962

4.  Specific interaction of the human immunodeficiency virus Tat proteins with a cellular protein kinase.

Authors:  C H Herrmann; A P Rice
Journal:  Virology       Date:  1993-12       Impact factor: 3.616

Review 5.  TBP, a universal eukaryotic transcription factor?

Authors:  N Hernandez
Journal:  Genes Dev       Date:  1993-07       Impact factor: 11.361

6.  Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator.

Authors:  R O Weinzierl; B D Dynlacht; R Tjian
Journal:  Nature       Date:  1993-04-08       Impact factor: 49.962

7.  Direct interaction of human TFIID with the HIV-1 transactivator tat.

Authors:  F Kashanchi; G Piras; M F Radonovich; J F Duvall; A Fattaey; C M Chiang; R G Roeder; J N Brady
Journal:  Nature       Date:  1994-01-20       Impact factor: 49.962

8.  Residues in the TATA-binding protein required to mediate a transcriptional response to retinoic acid in EC cells.

Authors:  M Keaveney; A Berkenstam; M Feigenbutz; G Vriend; H G Stunnenberg
Journal:  Nature       Date:  1993-10-07       Impact factor: 49.962

9.  Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment of DNA.

Authors:  M J Zoller; M Smith
Journal:  Nucleic Acids Res       Date:  1982-10-25       Impact factor: 16.971

10.  Both Arabidopsis TATA binding protein (TBP) isoforms are functionally identical in RNA polymerase II and III transcription in plant cells: evidence for gene-specific changes in DNA binding specificity of TBP.

Authors:  D J Heard; T Kiss; W Filipowicz
Journal:  EMBO J       Date:  1993-09       Impact factor: 11.598

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  7 in total

1.  FBI-1 can stimulate HIV-1 Tat activity and is targeted to a novel subnuclear domain that includes the Tat-P-TEFb-containing nuclear speckles.

Authors:  P Shannon Pendergrast; Chen Wang; Nouria Hernandez; Sui Huang
Journal:  Mol Biol Cell       Date:  2002-03       Impact factor: 4.138

Review 2.  Regulation of HIV-1 transcription.

Authors:  K A Roebuck; M Saifuddin
Journal:  Gene Expr       Date:  1999

3.  CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription.

Authors:  C Suñé; T Hayashi; Y Liu; W S Lane; R A Young; M A Garcia-Blanco
Journal:  Mol Cell Biol       Date:  1997-10       Impact factor: 4.272

4.  Purification and characterization of FBI-1, a cellular factor that binds to the human immunodeficiency virus type 1 inducer of short transcripts.

Authors:  F Pessler; P S Pendergrast; N Hernandez
Journal:  Mol Cell Biol       Date:  1997-07       Impact factor: 4.272

5.  RNA-targeted activators, but not DNA-targeted activators, repress the synthesis of short transcripts at the human immunodeficiency virus type 1 long terminal repeat.

Authors:  P S Pendergrast; N Hernandez
Journal:  J Virol       Date:  1997-02       Impact factor: 5.103

6.  Analysis of human immunodeficiency virus type 1 transcriptional elongation in resting CD4+ T cells in vivo.

Authors:  Kara G Lassen; Justin R Bailey; Robert F Siliciano
Journal:  J Virol       Date:  2004-09       Impact factor: 5.103

Review 7.  Tat gets the "green" light on transcription initiation.

Authors:  John Brady; Fatah Kashanchi
Journal:  Retrovirology       Date:  2005-11-09       Impact factor: 4.602

  7 in total

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